26S proteasome regulatory subunit 4 (PSMC1) is a 440-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P62191.
Explore in 3D Color by confidence AlphaFold DB UniProt
The mean pLDDT of this model is 77.8 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 13% |
| 70 to 90 | Confident: backbone generally right | 65% |
| 50 to 70 | Low: treat with caution | 11% |
| Below 50 | Very low: often disordered regions | 11% |
What pLDDT means and how to read it
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC1 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber…
Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases including PSMC1 and few additional components (PubMed:27342858, PubMed:27428775). Interacts with SCA7 (PubMed:11734547). Interacts with NGLY1…
Cytoplasm, Nucleus, Membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 9K53 | EM | 2.5 Å | B=1-440 |
| 8USD | EM | 2.7 Å | B=1-440 |
| 8USB | EM | 2.73 Å | B=1-440 |
| 9MBP | EM | 2.75 Å | B=1-440 |
| 9PDL | EM | 2.76 Å | B=1-440 |
| 9NKG | EM | 2.8 Å | B=1-440 |
| 9E8I | EM | 2.87 Å | B=1-440 |
| 9BV3 | EM | 2.9 Å | B=1-440 |
| 9E8H | EM | 2.9 Å | B=1-440 |
| 9K4J | EM | 2.9 Å | B=1-440 |
| 9NKF | EM | 2.9 Å | B=1-440 |
| 9U3L | EM | 2.91 Å | B=1-440 |
| 9NKI | EM | 2.94 Å | B=1-440 |
| 9PDI | EM | 2.98 Å | B=1-440 |
| 6MSB | EM | 3.0 Å | B=1-440 |
| 7W37 | EM | 3.0 Å | B=1-440 |
| 8CVT | EM | 3.0 Å | B=1-440 |
| 9E8G | EM | 3.01 Å | B=1-440 |
| 9PDN | EM | 3.04 Å | B=1-440 |
| 7W38 | EM | 3.1 Å | B=1-440 |
Showing 20 of 126 experimental structures (best resolution first).
MolViewer loads the AlphaFold model straight from AlphaFold DB into your browser. Show it as a cartoon, color by pLDDT, measure distances and angles, and load a PDB structure next to it to compare.